JOURNAL BROWSE
Search
Advanced SearchSearch Tips
Angiotensin I-converting Enzyme Inhibitory Activities of Porcine Skeletal Muscle Proteins Following Enzyme Digestion
facebook(new window)  Pirnt(new window) E-mail(new window) Excel Download
 Title & Authors
Angiotensin I-converting Enzyme Inhibitory Activities of Porcine Skeletal Muscle Proteins Following Enzyme Digestion
Katayama, K.; Fuchu, H.; Sakata, A.; Kawahara, S.; Yamauchi, K.; Kawamura, Y.; Muguruma, M.;
  PDF(new window)
 Abstract
Inhibitory activities against angiotensin I-converting enzyme (ACE) of enzymatic hydrolysates of porcine skeletal muscle proteins were investigated. Myosin B, myosin, actin, tropomyosin, troponin and water-soluble proteins extracted from pork loin were digested by eight kinds of proteases, including pepsin, -chymotrypsin, and trypsin. After digestion, hydrolysates produced from all proteins showed ACE inhibitory activities, and the peptic hydrolysate showed the strongest activity. In the case of myosin B, the molar concentration of peptic hydrolysate required to inhibit 50% of the activity increased gradually as digestion proceeded. The hydrolysates produced by sequential digestion with pepsin and -chymotrypsin, pepsin and trypsin or pepsin and pancreatin showed weaker activities than those by pepsin alone, suggesting that ACE inhibitory peptides from peptic digestion might lose their active sequences after digestion by the second protease. However, the hydrolysates produced by sequential digestion showed stronger activities than those by -chymotrypsin, trypsin or pancreatin alone. These results suggested that the hydrolysates of porcine meat were able to show ACE inhibitory activity, even if they were digested in vivo, and that pork might be a useful source of physiologically functional factors.
 Keywords
Angiotensin I-Converting Enzyme;Peptide;Porcine Skeletal Protein;Protease Digestion;
 Language
English
 Cited by
1.
Peptic Hydrolysate of Porcine Crude Myosin Has Many Active Fractions Inhibiting Angiotensin I-converting Enzyme,;;;;;;;

아세아태평양축산학회지, 2003. vol.16. 9, pp.1384-1389 crossref(new window)
2.
Attenuating Development of Cardiovascular Hypertrophy with Hydrolysate of Chicken Leg Bone Protein in Spontaneously Hypertensive Rats,;;;;;;

아세아태평양축산학회지, 2008. vol.21. 5, pp.732-737 crossref(new window)
 References
1.
Adibi, S., J. Klemencic and E. Philips. 1969. Metabolism of branched-chain amino acid in starvation. Clin. Res. 17:376.

2.
Arihara, K., Y. Nakashima, T. Mukai, T. Ishikawa and M. Itoh. 2001. Peptide inhibitors for angiotensin I-converting enzyme from enzymatic hydrolysates of porcine skeletal muscle proteins. Meat Sci. 57:319-324. crossref(new window)

3.
Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254. crossref(new window)

4.
Cheung, H. S., F. L. Wang, M. A. Ondetti, E. F. Sabo and D. W. Cushman. 1980. Binding of peptide substrate and inhibitors of angiotensin-converting enzyme. J. Biol. Chem. 255:401-407.

5.
Craft, I. L., D. Geddes, C. W. Hyde, I. J. Wise and D. M. Matthews. 1968. Absorption and malabsorption of glycine and glycine peptide in man. Gut 9:425-437. crossref(new window)

6.
Cushman, D. W. and H. S. Cheung. 1971. Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung. Biochem. Pharmacol. 20:1637-1648. crossref(new window)

7.
Eto, Y., T. Ito and S. Nishioka. 1999. Antihypertensive effect of alkaline protease hydrolysate of whey protein on blood pressure in spontaneously hypertensive rats. Nippon Eiyo Shokuryogaku kaishi 52:301-306. (in Japanese).

8.
Fujita, H., K. Yokoyama and M. Yoshikawa. 2000. Classification and antihypertensive activity of angiotensin I-converting enzyme inhibitory peptides derived from food proteins. J. Food Sci. 65:564-569. crossref(new window)

9.
Gornall, A. G., C. J. Bardawill and M. M. David. 1949. Determination of serum protein by means of the biuret reaction. J. Biol. Chem. 177:751-766.

10.
Hazra, A. K., S. P. Chock and R. W. Albers. 1984. Protein determination with trinitrobenzene sulfonate: a method relatively independent of amino acid composition. Anal. Biochem. 137:437-443. crossref(new window)

11.
Hattori, A. 1996. Niku no Kagaku, ed. by Okitani A. Asakura shoten, Tokyo, Japan. pp. 48-49

12.
Jimenez-Colmenero, F., J. Carballo and S. Cofrades. 2001. Healthier meat and meat products: their role as functional foods. Meat Sci. 59:5-13. crossref(new window)

13.
Joel, D. P. and A. S. James. 1982. Methods in Enzymology. Academic Press. New York. 85:164-171.

14.
Kawamura, Y., T. Sugimoto, T. Takane and M. Satake. 1989. Biologically active peptide derived from food proteins (I) Angiotensin-converting-enzyme inhibiting peptides from water-soluble protein of sardine muscle. Biryo Eiyouso Kenkyu 6:117-121. (in Japanese).

15.
Kawamura, Y., T. Takane, M. Satake and T. Sugimoto. 1992. Physiologically active peptide motif in proteins: Peptide inhibitor of ACE from the hydrolysates of antarctic krill muscle protein. J. Agric. Res. Quart. 26:210-213.

16.
Kohama, Y., S. Matsumoto, H. Oka, T. Teramoto, M. Okabe and T. Mimura. 1988. Isolation of angiotensin I converting enzyme inhibitor from tuna muscle. Biochem. Biophys. Res. Commun. 155:332-337. crossref(new window)

17.
Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685. crossref(new window)

18.
Li, D. F., X. H. Zhao, T. B. Yang, E. W. Johnson and P. A. Thacker. 1999. A comparison of the intestinal absorption of amino acids in piglets when provided in free form or as a dipeptide. Asian-Aust. J. Anim. Sci. 12:939-943.

19.
Lieberman, J. 1975. Elevation of serum angiotensin-convertingenzyme (ACE) level in sarcoidosis. Am. J. Med. 59:365-372. crossref(new window)

20.
Margossian, S. S. and S. Lowey. 1982. Methods in Enzymology. Academic Press. New York. 85:55-59.

21.
Maruyama, S., K. Nakagomi, N. Tomizuka and H. Suzuki. 1985. Angiotensin I-converting enzyme inhibitor derived from an enzymatic hydrolysate of casein. II. Isolation and bradykininpotentiating activity on the uterus and the ileum of rats. Agric. Biol. Chem. 49:1405-1409.

22.
Matsui, T., H. Matsufuji, E. Seki, K. Osajima, M. Nakashima and Y. Osajima. 1993. Inhibition of angiotensin I converting enzyme by Bacillus licheniformis alkaline protease hydrolysates derived from sardine muscle. Biosci. Biotech. Biochem. 57:922-925. crossref(new window)

23.
Matsumoto, K., A. Ogikubo, T. Yoshino, T. Matsui and Y. Osajima. 1994. Separation and purification of angiotensin I converting enzyme inhibitory peptide in peptic hydrolyzate of oyster. Nippon Shokuhin Kagaku Kogaku Kaishi 41:589-594. (in Japanese).

24.
Murphy, J. B. and M. W. Kies 1960. Note on spectrophotometric determination of proteins in dilute solutions. Biochim. Biophys. Acta 45:382-384. crossref(new window)

25.
Nakashima, Y., K. Arihara, A. Sasaki, H. Mio, S. Ishikawa and M. Itoh. 2002. Antihypertensive activities of peptides derived from porcine skeletal muscle myosin in spontaneously hypertensive rats. J. Food Sci. 67:434-437. crossref(new window)

26.
Ohta, T., A. Iwashita, S. Sasaki and Y. Kawamura. 1999. Antihypertensive action of the orally administered protease hydrolysates of chum salmon head and their angiotensin Iconverting enzyme inhibitory peptides. Food Sci. Technol. Int., Tokyo 3:339-343.

27.
Potter, J. D. 1982. Methods in Enzymology, Academic Press. New York. 85:241-249.

28.
Saito, Y., K. Wanezaki (Nakamura), A. Kawamoto and S. Imayasu. 1994. Structure and activity of angiotensin I converting enzyme inhibitory peptides from sake and sake lees. Biosci. Biotech. Biochem. 58:1767-1771. crossref(new window)

29.
Schagger, H. and G. Jagow. 1987. Tricine-sodium dodecyl sulfatepolyacrylamide gel electrophoresis for the separation of proteins in the range 1 to 100 kDa. Anal. Biochem. 166:368-379. crossref(new window)

30.
Smillie, L. B. 1982. Methods in Enzymology. Academic Press. New York. 85:234-237.

31.
Suetsuna, K. and K. Osajima. 1986. The Inhibitory activities against angiotensin I converting enzyme of basic peptides originating from sardine and hair tail meat. Nippon Suisan Gakkaishi 52:1981-1984. (in Japanese).

32.
Sugiyama, K., K. Takada, M. Egawa, I. Yamamoto, H. Onizuka and K. Oba. 1991. Hypertensive effect of fish protein hydrolysate. Nippon Nogeikagaku kaishi (in Japanese). 65:35-43.

33.
Szent-Gyorgyi, A. 1951. Chemistry of muscle contraction 2nd. ed. 151-152. Academic Press. New York

34.
Yamamoto, S., I. Toida and K. Iwai. 1980. Re-examination of the spectrophotometric assay for serum angiotensin-converting enzyme. Nippon Kyobu Shikkangaku Kaishi (in Japanese). 18:297-303.

35.
Yokoyama, K., H. Chiba and M. Yoshikawa. 1992. Peptide inhibitors for angiotensin I-converting enzyme from thermolysin digest of dried bonito. Biosci. Biotech. Biochem. 56:1541-1545. crossref(new window)

36.
Yoshii, H., N. Tachi, O. Sakamura, H. Takeyama, R. Ohba and T. Itani. 1999. Antihypertensive effect of oligo-peptide derived from hen's eggs. Nippon Shokuhin Kagaku Kogaku Kaishi 46: 45-50. (in Japanese).